June 2023
Volume 64, Issue 8
Open Access
ARVO Annual Meeting Abstract  |   June 2023
PLC-γ mediates FGF signaling to control lacrimal gland branching morphogenesis
Author Affiliations & Notes
  • Qian Wang
    Columbia University, New York, New York, United States
  • Xin Zhang
    Columbia University, New York, New York, United States
  • Footnotes
    Commercial Relationships   Qian Wang None; Xin Zhang None
  • Footnotes
    Support  1K99EY032171-01A1
Investigative Ophthalmology & Visual Science June 2023, Vol.64, 3292. doi:
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      Qian Wang, Xin Zhang; PLC-γ mediates FGF signaling to control lacrimal gland branching morphogenesis. Invest. Ophthalmol. Vis. Sci. 2023;64(8):3292.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose : The lacrimal gland is a tear-secreting organ that prevents dryness of the eyes. Seminal work established that fibroblast growth factor (FGF) signaling is essential for lacrimal gland development. Phospholipase C-γ (PLC-γ) is one of the handful substrates activated by FGF receptors through direct binding, but the physiological function of PLC-γ in lacrimal gland development is largely unexplored.

Methods : We generated conditional knockout mouse lines using Le-Cre, which is specifically expressed in the lacrimal gland epithelium and linked to an IRES-GFP reporter. We generated systemic mutant mouse lines by CRISPR/Cas9 genome editing techniques. GFP fluorescence and carmine staining were used to visualize lacrimal gland structure.

Results : Conditional knockout of PLC-γ1 caused lacrimal gland hyperplasia with ectopic branches from the primary duct as well as extra budding from the ventral side of the eye, consistent with a gain-of-function phenotype of FGF signaling. Immunostaining revealed an early onset of lacrimal gland differentiation in both acini and ducts. To investigate the mechanism by which PLC-γ is activated by FGFR signaling in vivo, we generated Fgfr2Y788F allele that lacks the PLC-γ binding site. Mouse carrying homozygous Fgfr2Y788F recapitulated the phenotype of extra-branching associated with PLC-γ1 mutant. In addition, inactivation of the PLC-γ N-terminal SH2 domain (PLC-γR586A) or the C-terminal SH2 domain (PLC-γR694A) mimicked PLC-γ null phenotype, suggesting that both SH2 domains are critical for PLC-γ function in lacrimal gland development.

Conclusions : Our study suggests that PLC-γ mediates FGFR signaling through both SH2 domains in lacrimal gland development.

This abstract was presented at the 2023 ARVO Annual Meeting, held in New Orleans, LA, April 23-27, 2023.

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